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LongText Report for: 5yzm-pdb

Name Class
5yzm-pdb
HEADER    HYDROLASE                               15-DEC-17   5YZM              
TITLE     CRYSTAL STRUCTURE OF S9 PEPTIDASE (INACTIVE FORM) FROM DEINOCOCCUS    
TITLE    2 RADIODURANS R1                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYL-PEPTIDE HYDROLASE, PUTATIVE;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: S9 PROLYL OLIGOPEPTIDASE;                                   
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS (STRAIN ATCC 13939 /    
SOURCE   3 DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 /    
SOURCE   4 VKM B-1422);                                                         
SOURCE   5 ORGANISM_TAXID: 243230;                                              
SOURCE   6 STRAIN: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / 
SOURCE   7 NCIMB 9279 / R1 / VKM B-1422;                                        
SOURCE   8 GENE: DR_0165;                                                       
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;                           
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PST50TR                                   
KEYWDS    SERINE PEPTIDASE, MEROPS S9, POP FAMILY, HYDROLASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.YADAV,S.N.JAMDAR,A.KUMAR,B.GHOSH,R.D.MAKDE                          
REVDAT   1   14-NOV-18 5YZM    0                                                
JRNL        AUTH   P.YADAV,S.N.JAMDAR,A.KUMAR,B.GHOSH,S.M.GOKHALE,R.D.MAKDE     
JRNL        TITL   CRYSTAL STRUCTURE OF S9C PEPTIDASE (S154A) MUTANT FROM       
JRNL        TITL 2 DEINOCOCCUS RADIODURANS R1                                   
JRNL        REF    J.BIOL.CHEM.                               2018              
JRNL        REFN                   ESSN 1083-351X                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 132060                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6534                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.8764 -  7.1385    0.98     4194   208  0.1644 0.1708        
REMARK   3     2  7.1385 -  5.6692    1.00     4180   227  0.1707 0.2033        
REMARK   3     3  5.6692 -  4.9534    1.00     4243   210  0.1469 0.1665        
REMARK   3     4  4.9534 -  4.5009    1.00     4203   216  0.1353 0.1474        
REMARK   3     5  4.5009 -  4.1786    1.00     4185   220  0.1443 0.1598        
REMARK   3     6  4.1786 -  3.9323    1.00     4184   221  0.1595 0.1911        
REMARK   3     7  3.9323 -  3.7355    0.99     4131   241  0.1746 0.1966        
REMARK   3     8  3.7355 -  3.5729    0.99     4205   208  0.1754 0.2049        
REMARK   3     9  3.5729 -  3.4354    0.99     4176   215  0.1911 0.2288        
REMARK   3    10  3.4354 -  3.3169    1.00     4146   228  0.1961 0.2272        
REMARK   3    11  3.3169 -  3.2132    1.00     4176   211  0.2066 0.2310        
REMARK   3    12  3.2132 -  3.1214    1.00     4201   233  0.2103 0.2633        
REMARK   3    13  3.1214 -  3.0392    1.00     4184   241  0.2099 0.2678        
REMARK   3    14  3.0392 -  2.9651    1.00     4212   184  0.2129 0.2443        
REMARK   3    15  2.9651 -  2.8977    1.00     4165   228  0.2121 0.2551        
REMARK   3    16  2.8977 -  2.8360    1.00     4159   218  0.2194 0.2671        
REMARK   3    17  2.8360 -  2.7793    1.00     4206   201  0.2294 0.2716        
REMARK   3    18  2.7793 -  2.7269    1.00     4187   236  0.2194 0.2496        
REMARK   3    19  2.7269 -  2.6782    1.00     4229   214  0.2242 0.2681        
REMARK   3    20  2.6782 -  2.6328    1.00     4116   205  0.2268 0.2782        
REMARK   3    21  2.6328 -  2.5903    1.00     4226   229  0.2253 0.2685        
REMARK   3    22  2.5903 -  2.5505    1.00     4181   200  0.2278 0.2491        
REMARK   3    23  2.5505 -  2.5130    1.00     4177   219  0.2312 0.2564        
REMARK   3    24  2.5130 -  2.4776    1.00     4198   230  0.2383 0.2946        
REMARK   3    25  2.4776 -  2.4441    1.00     4163   212  0.2348 0.2667        
REMARK   3    26  2.4441 -  2.4124    1.00     4240   204  0.2340 0.2725        
REMARK   3    27  2.4124 -  2.3822    1.00     4092   230  0.2448 0.2887        
REMARK   3    28  2.3822 -  2.3535    1.00     4259   203  0.2535 0.3130        
REMARK   3    29  2.3535 -  2.3261    1.00     4171   226  0.2624 0.3109        
REMARK   3    30  2.3261 -  2.3000    1.00     4137   216  0.2605 0.2849        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.300           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002          18928                                  
REMARK   3   ANGLE     :  0.578          25827                                  
REMARK   3   CHIRALITY :  0.043           2713                                  
REMARK   3   PLANARITY :  0.004           3432                                  
REMARK   3   DIHEDRAL  : 11.898          10873                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6556 -27.1590 -31.2665              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2591 T22:   0.3302                                     
REMARK   3      T33:   0.2789 T12:  -0.0096                                     
REMARK   3      T13:   0.0049 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0447 L22:   0.2978                                     
REMARK   3      L33:  -0.0206 L12:   0.0562                                     
REMARK   3      L13:   0.0070 L23:   0.0847                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0083 S12:  -0.0188 S13:  -0.0085                       
REMARK   3      S21:  -0.0025 S22:   0.0323 S23:   0.0236                       
REMARK   3      S31:  -0.0120 S32:  -0.0215 S33:  -0.0248                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5YZM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005998.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5-5.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : RRCAT INDUS-2                      
REMARK 200  BEAMLINE                       : PX-BL21                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97947                            
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 132199                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.770                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4HXE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM SODIUM ACETATE, PH 4.5, 200MM       
REMARK 280  SODIUM CHLORIDE, 10MM MAGNESIUM CHLORIDE, 12% PEG 3350, PH 5.47,    
REMARK 280  MICROBATCH, TEMPERATURE 294K                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       97.54600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     ASP A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     LYS A    46                                                      
REMARK 465     PRO A    47                                                      
REMARK 465     ASP A    48                                                      
REMARK 465     LYS A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     PHE A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     ARG A    53                                                      
REMARK 465     ALA A   143                                                      
REMARK 465     ASP A   144                                                      
REMARK 465     THR A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     ASP A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     ARG A   149                                                      
REMARK 465     ASP A   150                                                      
REMARK 465     GLU A   151                                                      
REMARK 465     ARG A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     VAL A   157                                                      
REMARK 465     LEU A   158                                                      
REMARK 465     THR A   159                                                      
REMARK 465     ARG A   160                                                      
REMARK 465     PRO A   161                                                      
REMARK 465     VAL A   162                                                      
REMARK 465     TYR A   163                                                      
REMARK 465     ARG A   164                                                      
REMARK 465     ALA A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     GLY A   167                                                      
REMARK 465     ALA A   168                                                      
REMARK 465     ASP A   169                                                      
REMARK 465     TRP A   170                                                      
REMARK 465     LEU A   171                                                      
REMARK 465     PRO A   172                                                      
REMARK 465     GLU A   173                                                      
REMARK 465     ALA A   236                                                      
REMARK 465     ASP A   237                                                      
REMARK 465     ALA A   238                                                      
REMARK 465     PRO A   239                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     ALA A   241                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     SER B    40                                                      
REMARK 465     GLU B    41                                                      
REMARK 465     GLU B    42                                                      
REMARK 465     ASP B    43                                                      
REMARK 465     PRO B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     LYS B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     ASP B    48                                                      
REMARK 465     LYS B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     PHE B    51                                                      
REMARK 465     ALA B    52                                                      
REMARK 465     ARG B    53                                                      
REMARK 465     ALA B   143                                                      
REMARK 465     ASP B   144                                                      
REMARK 465     THR B   145                                                      
REMARK 465     GLU B   146                                                      
REMARK 465     ASP B   147                                                      
REMARK 465     LYS B   148                                                      
REMARK 465     ARG B   149                                                      
REMARK 465     ASP B   150                                                      
REMARK 465     GLU B   151                                                      
REMARK 465     ARG B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     ALA B   155                                                      
REMARK 465     ARG B   156                                                      
REMARK 465     VAL B   157                                                      
REMARK 465     LEU B   158                                                      
REMARK 465     THR B   159                                                      
REMARK 465     ARG B   160                                                      
REMARK 465     PRO B   161                                                      
REMARK 465     VAL B   162                                                      
REMARK 465     TYR B   163                                                      
REMARK 465     ARG B   164                                                      
REMARK 465     ALA B   165                                                      
REMARK 465     ASN B   166                                                      
REMARK 465     GLY B   167                                                      
REMARK 465     ALA B   168                                                      
REMARK 465     ASP B   169                                                      
REMARK 465     TRP B   170                                                      
REMARK 465     LEU B   171                                                      
REMARK 465     PRO B   172                                                      
REMARK 465     GLU B   173                                                      
REMARK 465     ARG B   174                                                      
REMARK 465     ASP B   237                                                      
REMARK 465     ALA B   238                                                      
REMARK 465     PRO B   239                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     SER C    40                                                      
REMARK 465     GLU C    41                                                      
REMARK 465     GLU C    42                                                      
REMARK 465     ASP C    43                                                      
REMARK 465     PRO C    44                                                      
REMARK 465     ALA C    45                                                      
REMARK 465     LYS C    46                                                      
REMARK 465     PRO C    47                                                      
REMARK 465     ASP C    48                                                      
REMARK 465     LYS C    49                                                      
REMARK 465     ASP C    50                                                      
REMARK 465     PHE C    51                                                      
REMARK 465     ALA C    52                                                      
REMARK 465     GLY C    99                                                      
REMARK 465     GLU C   100                                                      
REMARK 465     VAL C   101                                                      
REMARK 465     ALA C   143                                                      
REMARK 465     ASP C   144                                                      
REMARK 465     THR C   145                                                      
REMARK 465     GLU C   146                                                      
REMARK 465     ASP C   147                                                      
REMARK 465     LYS C   148                                                      
REMARK 465     ARG C   149                                                      
REMARK 465     ASP C   150                                                      
REMARK 465     GLU C   151                                                      
REMARK 465     ARG C   152                                                      
REMARK 465     GLY C   153                                                      
REMARK 465     GLU C   154                                                      
REMARK 465     ALA C   155                                                      
REMARK 465     ARG C   156                                                      
REMARK 465     VAL C   157                                                      
REMARK 465     LEU C   158                                                      
REMARK 465     THR C   159                                                      
REMARK 465     ARG C   160                                                      
REMARK 465     PRO C   161                                                      
REMARK 465     VAL C   162                                                      
REMARK 465     TYR C   163                                                      
REMARK 465     ARG C   164                                                      
REMARK 465     ALA C   165                                                      
REMARK 465     ASN C   166                                                      
REMARK 465     GLY C   167                                                      
REMARK 465     ALA C   168                                                      
REMARK 465     ASP C   169                                                      
REMARK 465     TRP C   170                                                      
REMARK 465     LEU C   171                                                      
REMARK 465     PRO C   172                                                      
REMARK 465     GLU C   173                                                      
REMARK 465     ARG C   174                                                      
REMARK 465     PRO C   175                                                      
REMARK 465     THR C   235                                                      
REMARK 465     ALA C   236                                                      
REMARK 465     ASP C   237                                                      
REMARK 465     ALA C   238                                                      
REMARK 465     PRO C   239                                                      
REMARK 465     ALA C   240                                                      
REMARK 465     ALA C   241                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     ASN D     2                                                      
REMARK 465     ASN D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     PRO D     7                                                      
REMARK 465     SER D    40                                                      
REMARK 465     GLU D    41                                                      
REMARK 465     GLU D    42                                                      
REMARK 465     ASP D    43                                                      
REMARK 465     PRO D    44                                                      
REMARK 465     ALA D    45                                                      
REMARK 465     LYS D    46                                                      
REMARK 465     PRO D    47                                                      
REMARK 465     ASP D    48                                                      
REMARK 465     LYS D    49                                                      
REMARK 465     ASP D    50                                                      
REMARK 465     PHE D    51                                                      
REMARK 465     ALA D    52                                                      
REMARK 465     ALA D    98                                                      
REMARK 465     GLY D    99                                                      
REMARK 465     GLU D   100                                                      
REMARK 465     VAL D   101                                                      
REMARK 465     HIS D   120                                                      
REMARK 465     THR D   142                                                      
REMARK 465     ALA D   143                                                      
REMARK 465     ASP D   144                                                      
REMARK 465     THR D   145                                                      
REMARK 465     GLU D   146                                                      
REMARK 465     ASP D   147                                                      
REMARK 465     LYS D   148                                                      
REMARK 465     ARG D   149                                                      
REMARK 465     ASP D   150                                                      
REMARK 465     GLU D   151                                                      
REMARK 465     ARG D   152                                                      
REMARK 465     GLY D   153                                                      
REMARK 465     GLU D   154                                                      
REMARK 465     ALA D   155                                                      
REMARK 465     ARG D   156                                                      
REMARK 465     VAL D   157                                                      
REMARK 465     LEU D   158                                                      
REMARK 465     THR D   159                                                      
REMARK 465     ARG D   160                                                      
REMARK 465     PRO D   161                                                      
REMARK 465     VAL D   162                                                      
REMARK 465     TYR D   163                                                      
REMARK 465     ARG D   164                                                      
REMARK 465     ALA D   165                                                      
REMARK 465     ASN D   166                                                      
REMARK 465     GLY D   167                                                      
REMARK 465     ALA D   168                                                      
REMARK 465     ASP D   169                                                      
REMARK 465     TRP D   170                                                      
REMARK 465     LEU D   171                                                      
REMARK 465     PRO D   172                                                      
REMARK 465     GLU D   173                                                      
REMARK 465     ARG D   174                                                      
REMARK 465     PRO D   175                                                      
REMARK 465     ALA D   236                                                      
REMARK 465     ASP D   237                                                      
REMARK 465     ALA D   238                                                      
REMARK 465     PRO D   239                                                      
REMARK 465     ALA D   240                                                      
REMARK 465     ALA D   241                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A  73    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 100    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 102    CG   CD   CE   NZ                                   
REMARK 470     LYS A 111    CG   CD   CE   NZ                                   
REMARK 470     LYS A 122    CG   CD   CE   NZ                                   
REMARK 470     ARG A 174    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 184    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 187    NZ                                                  
REMARK 470     TRP A 224    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 224    CZ3  CH2                                            
REMARK 470     THR A 235    OG1                                                 
REMARK 470     GLN A 243    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 347    CG   CD   CE   NZ                                   
REMARK 470     GLU A 421    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 495    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 554    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B  73    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B  75    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 100    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 102    CG   CD   CE   NZ                                   
REMARK 470     LYS B 111    CG   CD   CE   NZ                                   
REMARK 470     LYS B 122    CG   CD   CE   NZ                                   
REMARK 470     ARG B 135    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     GLU B 195    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 218    CG   CD   OE1  OE2                                  
REMARK 470     TRP B 219    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 219    CZ3  CH2                                            
REMARK 470     GLN B 220    CG   CD   OE1  NE2                                  
REMARK 470     TRP B 224    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 224    CZ3  CH2                                            
REMARK 470     ARG B 225    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 243    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 273    CG   CD   CE   NZ                                   
REMARK 470     LYS B 347    CG   CD   CE   NZ                                   
REMARK 470     ARG B 566    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  30    CG   CD   CE   NZ                                   
REMARK 470     ARG C  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 102    CG   CD   CE   NZ                                   
REMARK 470     LYS C 111    CG   CD   CE   NZ                                   
REMARK 470     GLU C 114    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 116    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS C 120    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 122    CG   CD   CE   NZ                                   
REMARK 470     ARG C 135    CZ   NH1  NH2                                       
REMARK 470     TRP C 179    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 179    CZ3  CH2                                            
REMARK 470     GLU C 184    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 187    CG   CD   CE   NZ                                   
REMARK 470     GLU C 195    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 217    CG   OD1  OD2                                       
REMARK 470     GLU C 218    CG   CD   OE1  OE2                                  
REMARK 470     TRP C 219    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP C 219    CZ3  CH2                                            
REMARK 470     GLN C 220    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 288    CG   CD   OE1  NE2                                  
REMARK 470     ASP C 323    CG   OD1  OD2                                       
REMARK 470     LYS C 347    CG   CD   CE   NZ                                   
REMARK 470     ARG C 376    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 421    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 424    CG   CD   OE1  NE2                                  
REMARK 470     LYS D  30    CG   CD   CE   NZ                                   
REMARK 470     ARG D  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 102    CG   CD   CE   NZ                                   
REMARK 470     GLU D 114    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 116    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 122    CG   CD   CE   NZ                                   
REMARK 470     ARG D 135    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 184    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 187    CG   CD   CE   NZ                                   
REMARK 470     ARG D 189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 195    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 218    CG   CD   OE1  OE2                                  
REMARK 470     TRP D 219    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 219    CZ3  CH2                                            
REMARK 470     GLN D 220    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 223    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 243    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 244    CG   CD   CE   NZ                                   
REMARK 470     ASP D 323    CG   OD1  OD2                                       
REMARK 470     GLU D 364    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 421    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 103      101.86   -164.54                                   
REMARK 500    SER A 250     -169.14   -161.68                                   
REMARK 500    GLN A 262      -55.17   -121.41                                   
REMARK 500    ASP A 293       58.78    -95.16                                   
REMARK 500    ASP A 350       89.99   -156.71                                   
REMARK 500    ARG A 480       49.50   -147.64                                   
REMARK 500    THR A 483      -94.21   -104.22                                   
REMARK 500    SER A 514     -115.78     58.99                                   
REMARK 500    ALA B  98     -162.95   -111.23                                   
REMARK 500    ALA B 103      104.84   -165.49                                   
REMARK 500    GLN B 262      -55.53   -120.83                                   
REMARK 500    ASP B 293       55.92    -93.76                                   
REMARK 500    ARG B 480       49.05   -148.42                                   
REMARK 500    THR B 483      -94.55   -105.86                                   
REMARK 500    SER B 514     -114.19     58.45                                   
REMARK 500    ALA C 103      106.59   -165.28                                   
REMARK 500    ASP C 293       57.19    -93.62                                   
REMARK 500    ASP C 350       89.47   -156.81                                   
REMARK 500    ARG C 480       48.98   -149.00                                   
REMARK 500    THR C 483      -94.27   -104.12                                   
REMARK 500    SER C 514     -115.74     59.05                                   
REMARK 500    ALA D 103      107.52   -166.24                                   
REMARK 500    GLN D 262      -54.38   -121.48                                   
REMARK 500    ASP D 293       57.53    -94.95                                   
REMARK 500    ASP D 350       89.41   -157.32                                   
REMARK 500    ARG D 480       50.22   -148.72                                   
REMARK 500    THR D 483      -93.36   -103.27                                   
REMARK 500    SER D 514     -115.43     58.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1105        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH B1127        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH D 998        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH D 999        DISTANCE =  6.78 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 701                 
DBREF  5YZM A    2   655  UNP    Q9RXY9   Q9RXY9_DEIRA     2    655             
DBREF  5YZM B    2   655  UNP    Q9RXY9   Q9RXY9_DEIRA     2    655             
DBREF  5YZM C    2   655  UNP    Q9RXY9   Q9RXY9_DEIRA     2    655             
DBREF  5YZM D    2   655  UNP    Q9RXY9   Q9RXY9_DEIRA     2    655             
SEQADV 5YZM GLY A    0  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 5YZM SER A    1  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 5YZM GLY B    0  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 5YZM SER B    1  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 5YZM GLY C    0  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 5YZM SER C    1  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 5YZM GLY D    0  UNP  Q9RXY9              EXPRESSION TAG                 
SEQADV 5YZM SER D    1  UNP  Q9RXY9              EXPRESSION TAG                 
SEQRES   1 A  656  GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP          
SEQRES   2 A  656  SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL          
SEQRES   3 A  656  SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN          
SEQRES   4 A  656  ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE          
SEQRES   5 A  656  ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU          
SEQRES   6 A  656  GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY          
SEQRES   7 A  656  ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN          
SEQRES   8 A  656  ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA          
SEQRES   9 A  656  ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG          
SEQRES  10 A  656  ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN          
SEQRES  11 A  656  TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR          
SEQRES  12 A  656  ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA          
SEQRES  13 A  656  ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA          
SEQRES  14 A  656  ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR          
SEQRES  15 A  656  ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO          
SEQRES  16 A  656  GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER          
SEQRES  17 A  656  ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN          
SEQRES  18 A  656  ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU          
SEQRES  19 A  656  PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU          
SEQRES  20 A  656  ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO          
SEQRES  21 A  656  ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY          
SEQRES  22 A  656  LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU          
SEQRES  23 A  656  ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS          
SEQRES  24 A  656  PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY          
SEQRES  25 A  656  ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR          
SEQRES  26 A  656  LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU          
SEQRES  27 A  656  PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP          
SEQRES  28 A  656  HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN          
SEQRES  29 A  656  GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG          
SEQRES  30 A  656  PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP          
SEQRES  31 A  656  LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN          
SEQRES  32 A  656  ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY          
SEQRES  33 A  656  TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA          
SEQRES  34 A  656  LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY          
SEQRES  35 A  656  HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG          
SEQRES  36 A  656  GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL          
SEQRES  37 A  656  GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG          
SEQRES  38 A  656  TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE          
SEQRES  39 A  656  ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA          
SEQRES  40 A  656  LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET          
SEQRES  41 A  656  THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA          
SEQRES  42 A  656  ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE          
SEQRES  43 A  656  GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP          
SEQRES  44 A  656  GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU          
SEQRES  45 A  656  LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN          
SEQRES  46 A  656  VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP          
SEQRES  47 A  656  HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA          
SEQRES  48 A  656  ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG          
SEQRES  49 A  656  PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG          
SEQRES  50 A  656  PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA          
SEQRES  51 A  656  TRP LEU GLU ARG TRP LEU                                      
SEQRES   1 B  656  GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP          
SEQRES   2 B  656  SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL          
SEQRES   3 B  656  SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN          
SEQRES   4 B  656  ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE          
SEQRES   5 B  656  ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU          
SEQRES   6 B  656  GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY          
SEQRES   7 B  656  ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN          
SEQRES   8 B  656  ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA          
SEQRES   9 B  656  ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG          
SEQRES  10 B  656  ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN          
SEQRES  11 B  656  TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR          
SEQRES  12 B  656  ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA          
SEQRES  13 B  656  ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA          
SEQRES  14 B  656  ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR          
SEQRES  15 B  656  ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO          
SEQRES  16 B  656  GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER          
SEQRES  17 B  656  ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN          
SEQRES  18 B  656  ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU          
SEQRES  19 B  656  PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU          
SEQRES  20 B  656  ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO          
SEQRES  21 B  656  ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY          
SEQRES  22 B  656  LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU          
SEQRES  23 B  656  ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS          
SEQRES  24 B  656  PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY          
SEQRES  25 B  656  ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR          
SEQRES  26 B  656  LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU          
SEQRES  27 B  656  PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP          
SEQRES  28 B  656  HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN          
SEQRES  29 B  656  GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG          
SEQRES  30 B  656  PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP          
SEQRES  31 B  656  LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN          
SEQRES  32 B  656  ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY          
SEQRES  33 B  656  TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA          
SEQRES  34 B  656  LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY          
SEQRES  35 B  656  HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG          
SEQRES  36 B  656  GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL          
SEQRES  37 B  656  GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG          
SEQRES  38 B  656  TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE          
SEQRES  39 B  656  ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA          
SEQRES  40 B  656  LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET          
SEQRES  41 B  656  THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA          
SEQRES  42 B  656  ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE          
SEQRES  43 B  656  GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP          
SEQRES  44 B  656  GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU          
SEQRES  45 B  656  LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN          
SEQRES  46 B  656  VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP          
SEQRES  47 B  656  HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA          
SEQRES  48 B  656  ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG          
SEQRES  49 B  656  PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG          
SEQRES  50 B  656  PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA          
SEQRES  51 B  656  TRP LEU GLU ARG TRP LEU                                      
SEQRES   1 C  656  GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP          
SEQRES   2 C  656  SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL          
SEQRES   3 C  656  SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN          
SEQRES   4 C  656  ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE          
SEQRES   5 C  656  ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU          
SEQRES   6 C  656  GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY          
SEQRES   7 C  656  ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN          
SEQRES   8 C  656  ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA          
SEQRES   9 C  656  ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG          
SEQRES  10 C  656  ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN          
SEQRES  11 C  656  TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR          
SEQRES  12 C  656  ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA          
SEQRES  13 C  656  ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA          
SEQRES  14 C  656  ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR          
SEQRES  15 C  656  ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO          
SEQRES  16 C  656  GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER          
SEQRES  17 C  656  ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN          
SEQRES  18 C  656  ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU          
SEQRES  19 C  656  PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU          
SEQRES  20 C  656  ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO          
SEQRES  21 C  656  ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY          
SEQRES  22 C  656  LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU          
SEQRES  23 C  656  ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS          
SEQRES  24 C  656  PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY          
SEQRES  25 C  656  ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR          
SEQRES  26 C  656  LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU          
SEQRES  27 C  656  PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP          
SEQRES  28 C  656  HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN          
SEQRES  29 C  656  GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG          
SEQRES  30 C  656  PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP          
SEQRES  31 C  656  LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN          
SEQRES  32 C  656  ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY          
SEQRES  33 C  656  TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA          
SEQRES  34 C  656  LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY          
SEQRES  35 C  656  HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG          
SEQRES  36 C  656  GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL          
SEQRES  37 C  656  GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG          
SEQRES  38 C  656  TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE          
SEQRES  39 C  656  ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA          
SEQRES  40 C  656  LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET          
SEQRES  41 C  656  THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA          
SEQRES  42 C  656  ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE          
SEQRES  43 C  656  GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP          
SEQRES  44 C  656  GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU          
SEQRES  45 C  656  LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN          
SEQRES  46 C  656  VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP          
SEQRES  47 C  656  HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA          
SEQRES  48 C  656  ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG          
SEQRES  49 C  656  PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG          
SEQRES  50 C  656  PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA          
SEQRES  51 C  656  TRP LEU GLU ARG TRP LEU                                      
SEQRES   1 D  656  GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP          
SEQRES   2 D  656  SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL          
SEQRES   3 D  656  SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN          
SEQRES   4 D  656  ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE          
SEQRES   5 D  656  ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU          
SEQRES   6 D  656  GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY          
SEQRES   7 D  656  ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN          
SEQRES   8 D  656  ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA          
SEQRES   9 D  656  ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG          
SEQRES  10 D  656  ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN          
SEQRES  11 D  656  TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR          
SEQRES  12 D  656  ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA          
SEQRES  13 D  656  ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA          
SEQRES  14 D  656  ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR          
SEQRES  15 D  656  ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO          
SEQRES  16 D  656  GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER          
SEQRES  17 D  656  ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN          
SEQRES  18 D  656  ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU          
SEQRES  19 D  656  PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU          
SEQRES  20 D  656  ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO          
SEQRES  21 D  656  ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY          
SEQRES  22 D  656  LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU          
SEQRES  23 D  656  ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS          
SEQRES  24 D  656  PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY          
SEQRES  25 D  656  ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR          
SEQRES  26 D  656  LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU          
SEQRES  27 D  656  PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP          
SEQRES  28 D  656  HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN          
SEQRES  29 D  656  GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG          
SEQRES  30 D  656  PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP          
SEQRES  31 D  656  LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN          
SEQRES  32 D  656  ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY          
SEQRES  33 D  656  TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA          
SEQRES  34 D  656  LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY          
SEQRES  35 D  656  HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG          
SEQRES  36 D  656  GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL          
SEQRES  37 D  656  GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG          
SEQRES  38 D  656  TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE          
SEQRES  39 D  656  ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA          
SEQRES  40 D  656  LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET          
SEQRES  41 D  656  THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA          
SEQRES  42 D  656  ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE          
SEQRES  43 D  656  GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP          
SEQRES  44 D  656  GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU          
SEQRES  45 D  656  LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN          
SEQRES  46 D  656  VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP          
SEQRES  47 D  656  HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA          
SEQRES  48 D  656  ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG          
SEQRES  49 D  656  PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG          
SEQRES  50 D  656  PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA          
SEQRES  51 D  656  TRP LEU GLU ARG TRP LEU                                      
HET    ACT  A 701       4                                                       
HET    ACT  B 701       4                                                       
HET    ACT  C 701       4                                                       
HET    ACT  D 701       4                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   5  ACT    4(C2 H3 O2 1-)                                               
FORMUL   9  HOH   *1052(H2 O)                                                   
HELIX    1 AA1 GLY A   10  LEU A   17  5                                   8    
HELIX    2 AA2 ASP A  217  GLN A  223  1                                   7    
HELIX    3 AA3 LEU A  390  PHE A  394  5                                   5    
HELIX    4 AA4 THR A  445  ARG A  454  1                                  10    
HELIX    5 AA5 GLY A  470  ALA A  476  1                                   7    
HELIX    6 AA6 THR A  483  VAL A  500  1                                  18    
HELIX    7 AA7 SER A  514  GLY A  525  1                                  12    
HELIX    8 AA8 ASN A  541  SER A  549  1                                   9    
HELIX    9 AA9 ILE A  551  GLY A  561  1                                  11    
HELIX   10 AB1 ARG A  566  LEU A  576  1                                  11    
HELIX   11 AB2 SER A  577  VAL A  585  5                                   9    
HELIX   12 AB3 VAL A  602  HIS A  615  1                                  14    
HELIX   13 AB4 HIS A  629  GLY A  635  1                                   7    
HELIX   14 AB5 PRO A  637  LEU A  655  1                                  19    
HELIX   15 AB6 GLY B   10  LEU B   17  5                                   8    
HELIX   16 AB7 ASP B  217  GLN B  223  1                                   7    
HELIX   17 AB8 LEU B  390  PHE B  394  5                                   5    
HELIX   18 AB9 THR B  445  ARG B  454  1                                  10    
HELIX   19 AC1 GLY B  470  ALA B  476  1                                   7    
HELIX   20 AC2 THR B  483  VAL B  500  1                                  18    
HELIX   21 AC3 SER B  514  GLY B  525  1                                  12    
HELIX   22 AC4 ASN B  541  SER B  549  1                                   9    
HELIX   23 AC5 ILE B  551  GLY B  561  1                                  11    
HELIX   24 AC6 ARG B  566  LEU B  576  1                                  11    
HELIX   25 AC7 SER B  577  VAL B  585  5                                   9    
HELIX   26 AC8 VAL B  602  HIS B  615  1                                  14    
HELIX   27 AC9 HIS B  629  GLY B  635  1                                   7    
HELIX   28 AD1 PRO B  637  LEU B  655  1                                  19    
HELIX   29 AD2 GLY C   10  LEU C   17  5                                   8    
HELIX   30 AD3 ASP C  217  GLN C  223  1                                   7    
HELIX   31 AD4 LEU C  390  PHE C  394  5                                   5    
HELIX   32 AD5 THR C  445  ARG C  454  1                                  10    
HELIX   33 AD6 GLY C  470  ALA C  476  1                                   7    
HELIX   34 AD7 THR C  483  VAL C  500  1                                  18    
HELIX   35 AD8 SER C  514  GLY C  525  1                                  12    
HELIX   36 AD9 ASN C  541  SER C  549  1                                   9    
HELIX   37 AE1 ILE C  551  GLY C  561  1                                  11    
HELIX   38 AE2 ARG C  566  LEU C  576  1                                  11    
HELIX   39 AE3 SER C  577  VAL C  585  5                                   9    
HELIX   40 AE4 VAL C  602  HIS C  615  1                                  14    
HELIX   41 AE5 HIS C  629  GLY C  635  1                                   7    
HELIX   42 AE6 PRO C  637  LEU C  655  1                                  19    
HELIX   43 AE7 GLY D   10  LEU D   17  5                                   8    
HELIX   44 AE8 ASP D  217  GLN D  223  1                                   7    
HELIX   45 AE9 LEU D  390  PHE D  394  5                                   5    
HELIX   46 AF1 THR D  445  ARG D  454  1                                  10    
HELIX   47 AF2 GLY D  470  ALA D  476  1                                   7    
HELIX   48 AF3 THR D  483  VAL D  500  1                                  18    
HELIX   49 AF4 SER D  514  GLY D  525  1                                  12    
HELIX   50 AF5 ASN D  541  SER D  549  1                                   9    
HELIX   51 AF6 ILE D  551  GLY D  561  1                                  11    
HELIX   52 AF7 ARG D  566  LEU D  576  1                                  11    
HELIX   53 AF8 SER D  577  VAL D  585  5                                   9    
HELIX   54 AF9 VAL D  602  HIS D  615  1                                  14    
HELIX   55 AG1 HIS D  629  GLY D  635  1                                   7    
HELIX   56 AG2 PRO D  637  LEU D  655  1                                  19    
SHEET    1 AA1 4 PHE A  19  VAL A  25  0                                        
SHEET    2 AA1 4 VAL A  32  ILE A  39 -1  O  ALA A  33   N  GLN A  24           
SHEET    3 AA1 4 TYR A  56  SER A  63 -1  O  TRP A  61   N  PHE A  34           
SHEET    4 AA1 4 ARG A  69  PRO A  70 -1  O  ARG A  69   N  LEU A  62           
SHEET    1 AA2 4 GLY A  79  TRP A  85  0                                        
SHEET    2 AA2 4 ASN A  91  ALA A  98 -1  O  ALA A  93   N  ARG A  84           
SHEET    3 AA2 4 VAL A 101  PRO A 109 -1  O  VAL A 101   N  ALA A  98           
SHEET    4 AA2 4 ARG A 116  ARG A 117 -1  O  ARG A 116   N  LEU A 107           
SHEET    1 AA3 4 VAL A 125  TRP A 130  0                                        
SHEET    2 AA3 4 PHE A 136  THR A 141 -1  O  ALA A 138   N  GLN A 129           
SHEET    3 AA3 4 ALA A 177  ASP A 182 -1  O  TRP A 179   N  PHE A 139           
SHEET    4 AA3 4 LYS A 187  TYR A 192 -1  O  LYS A 187   N  ASP A 182           
SHEET    1 AA4 4 ILE A 198  TRP A 203  0                                        
SHEET    2 AA4 4 GLY A 209  GLN A 214 -1  O  VAL A 213   N  GLY A 199           
SHEET    3 AA4 4 GLN A 226  PRO A 232 -1  O  ASP A 227   N  GLN A 214           
SHEET    4 AA4 4 GLN A 243  SER A 250 -1  O  LEU A 245   N  VAL A 228           
SHEET    1 AA5 4 ALA A 252  PRO A 257  0                                        
SHEET    2 AA5 4 PHE A 264  GLY A 268 -1  O  ILE A 267   N  HIS A 253           
SHEET    3 AA5 4 HIS A 280  GLU A 285 -1  O  ILE A 284   N  PHE A 264           
SHEET    4 AA5 4 GLN A 288  ARG A 291 -1  O  ARG A 290   N  LEU A 283           
SHEET    1 AA6 4 ARG A 318  TRP A 319  0                                        
SHEET    2 AA6 4 THR A 324  VAL A 331 -1  O  LEU A 326   N  ARG A 318           
SHEET    3 AA6 4 SER A 334  HIS A 341 -1  O  PHE A 338   N  PHE A 327           
SHEET    4 AA6 4 GLY A 344  ASP A 350 -1  O  ASP A 350   N  LEU A 337           
SHEET    1 AA7 4 GLY A 355  ALA A 362  0                                        
SHEET    2 AA7 4 VAL A 367  SER A 373 -1  O  GLU A 372   N  VAL A 356           
SHEET    3 AA7 4 ARG A 376  LEU A 382 -1  O  GLU A 381   N  LEU A 369           
SHEET    4 AA7 4 GLN A 385  ARG A 386 -1  O  GLN A 385   N  LEU A 382           
SHEET    1 AA8 8 GLN A 402  THR A 408  0                                        
SHEET    2 AA8 8 GLY A 411  LEU A 418 -1  O  GLY A 413   N  PHE A 406           
SHEET    3 AA8 8 GLY A 457  SER A 461 -1  O  TYR A 460   N  TRP A 416           
SHEET    4 AA8 8 VAL A 426  ILE A 432  1  N  LEU A 429   O  GLY A 457           
SHEET    5 AA8 8 LEU A 503  GLY A 513  1  O  ALA A 509   N  LEU A 430           
SHEET    6 AA8 8 ALA A 532  ASP A 536  1  O  ASP A 536   N  GLY A 512           
SHEET    7 AA8 8 THR A 589  SER A 594  1  O  LEU A 590   N  ALA A 533           
SHEET    8 AA8 8 VAL A 619  PHE A 624  1  O  ARG A 620   N  ILE A 591           
SHEET    1 AA9 4 PHE B  19  VAL B  25  0                                        
SHEET    2 AA9 4 VAL B  32  GLN B  38 -1  O  ALA B  33   N  GLN B  24           
SHEET    3 AA9 4 ARG B  57  SER B  63 -1  O  ARG B  57   N  GLN B  38           
SHEET    4 AA9 4 ARG B  69  PRO B  70 -1  O  ARG B  69   N  LEU B  62           
SHEET    1 AB1 4 GLY B  79  TRP B  85  0                                        
SHEET    2 AB1 4 ASN B  91  SER B  97 -1  O  ALA B  93   N  ARG B  84           
SHEET    3 AB1 4 ALA B 104  PRO B 109 -1  O  MET B 106   N  PHE B  94           
SHEET    4 AB1 4 ARG B 116  ARG B 117 -1  O  ARG B 116   N  LEU B 107           
SHEET    1 AB2 4 VAL B 125  TRP B 130  0                                        
SHEET    2 AB2 4 PHE B 136  THR B 141 -1  O  ALA B 138   N  GLN B 129           
SHEET    3 AB2 4 ALA B 177  ASP B 182 -1  O  TRP B 179   N  PHE B 139           
SHEET    4 AB2 4 LYS B 187  TYR B 192 -1  O  LYS B 187   N  ASP B 182           
SHEET    1 AB3 4 LEU B 201  TRP B 203  0                                        
SHEET    2 AB3 4 GLY B 209  GLN B 214 -1  O  LEU B 211   N  SER B 202           
SHEET    3 AB3 4 GLN B 226  PRO B 232 -1  O  TYR B 229   N  ILE B 212           
SHEET    4 AB3 4 GLN B 243  SER B 250 -1  O  GLN B 243   N  ASP B 230           
SHEET    1 AB4 4 ALA B 252  PRO B 257  0                                        
SHEET    2 AB4 4 PHE B 264  GLY B 268 -1  O  ILE B 267   N  HIS B 253           
SHEET    3 AB4 4 HIS B 280  GLU B 285 -1  O  ILE B 284   N  PHE B 264           
SHEET    4 AB4 4 GLN B 288  ARG B 291 -1  O  ARG B 290   N  LEU B 283           
SHEET    1 AB5 4 ARG B 318  TRP B 319  0                                        
SHEET    2 AB5 4 THR B 324  VAL B 331 -1  O  LEU B 326   N  ARG B 318           
SHEET    3 AB5 4 SER B 334  HIS B 341 -1  O  PHE B 338   N  PHE B 327           
SHEET    4 AB5 4 VAL B 346  ASP B 350 -1  O  ASP B 350   N  LEU B 337           
SHEET    1 AB6 4 GLY B 355  ALA B 362  0                                        
SHEET    2 AB6 4 VAL B 367  SER B 373 -1  O  GLU B 372   N  VAL B 356           
SHEET    3 AB6 4 ARG B 376  LEU B 382 -1  O  GLU B 381   N  LEU B 369           
SHEET    4 AB6 4 GLN B 385  ARG B 386 -1  O  GLN B 385   N  LEU B 382           
SHEET    1 AB7 8 GLN B 402  THR B 408  0                                        
SHEET    2 AB7 8 GLY B 411  LEU B 418 -1  O  GLY B 413   N  PHE B 406           
SHEET    3 AB7 8 GLY B 457  SER B 461 -1  O  TYR B 460   N  TRP B 416           
SHEET    4 AB7 8 VAL B 426  ILE B 432  1  N  ASN B 431   O  CYS B 459           
SHEET    5 AB7 8 LEU B 503  GLY B 513  1  O  ALA B 509   N  LEU B 430           
SHEET    6 AB7 8 ALA B 532  ASP B 536  1  O  ASP B 536   N  GLY B 512           
SHEET    7 AB7 8 THR B 589  SER B 594  1  O  LEU B 590   N  ALA B 533           
SHEET    8 AB7 8 VAL B 619  PHE B 624  1  O  ARG B 620   N  ILE B 591           
SHEET    1 AB8 4 PHE C  19  VAL C  25  0                                        
SHEET    2 AB8 4 VAL C  32  GLN C  38 -1  O  ALA C  33   N  GLN C  24           
SHEET    3 AB8 4 ARG C  57  SER C  63 -1  O  TRP C  61   N  PHE C  34           
SHEET    4 AB8 4 ARG C  69  PRO C  70 -1  O  ARG C  69   N  LEU C  62           
SHEET    1 AB9 4 GLY C  79  TRP C  85  0                                        
SHEET    2 AB9 4 ASN C  91  SER C  97 -1  O  ALA C  93   N  ARG C  84           
SHEET    3 AB9 4 ALA C 104  PRO C 109 -1  O  MET C 106   N  PHE C  94           
SHEET    4 AB9 4 ARG C 116  ARG C 117 -1  O  ARG C 116   N  LEU C 107           
SHEET    1 AC1 4 SER C 126  TRP C 130  0                                        
SHEET    2 AC1 4 PHE C 136  THR C 141 -1  O  ALA C 138   N  GLN C 129           
SHEET    3 AC1 4 ALA C 177  ASP C 182 -1  O  TRP C 179   N  PHE C 139           
SHEET    4 AC1 4 LYS C 187  TYR C 192 -1  O  TYR C 192   N  LEU C 178           
SHEET    1 AC2 4 LEU C 201  TRP C 203  0                                        
SHEET    2 AC2 4 GLY C 209  GLN C 214 -1  O  LEU C 211   N  SER C 202           
SHEET    3 AC2 4 GLN C 226  PRO C 232 -1  O  TYR C 229   N  ILE C 212           
SHEET    4 AC2 4 GLN C 243  SER C 250 -1  O  LEU C 245   N  VAL C 228           
SHEET    1 AC3 4 ALA C 252  PRO C 257  0                                        
SHEET    2 AC3 4 PHE C 264  GLY C 268 -1  O  ILE C 267   N  HIS C 253           
SHEET    3 AC3 4 HIS C 280  GLU C 285 -1  O  ILE C 284   N  PHE C 264           
SHEET    4 AC3 4 GLN C 288  ARG C 291 -1  O  GLN C 288   N  GLU C 285           
SHEET    1 AC4 4 ARG C 318  TRP C 319  0                                        
SHEET    2 AC4 4 THR C 324  VAL C 331 -1  O  LEU C 326   N  ARG C 318           
SHEET    3 AC4 4 SER C 334  HIS C 341 -1  O  PHE C 338   N  PHE C 327           
SHEET    4 AC4 4 VAL C 346  ASP C 350 -1  O  ASP C 350   N  LEU C 337           
SHEET    1 AC5 4 GLY C 355  ALA C 362  0                                        
SHEET    2 AC5 4 VAL C 367  SER C 373 -1  O  GLU C 372   N  VAL C 356           
SHEET    3 AC5 4 ARG C 376  LEU C 382 -1  O  GLU C 381   N  LEU C 369           
SHEET    4 AC5 4 GLN C 385  ARG C 386 -1  O  GLN C 385   N  LEU C 382           
SHEET    1 AC6 8 GLN C 402  THR C 408  0                                        
SHEET    2 AC6 8 GLY C 411  LEU C 418 -1  O  GLY C 413   N  PHE C 406           
SHEET    3 AC6 8 GLY C 457  SER C 461 -1  O  TYR C 460   N  TRP C 416           
SHEET    4 AC6 8 VAL C 426  ILE C 432  1  N  LEU C 429   O  GLY C 457           
SHEET    5 AC6 8 LEU C 503  GLY C 513  1  O  ALA C 509   N  LEU C 430           
SHEET    6 AC6 8 ALA C 532  ASP C 536  1  O  ASP C 536   N  GLY C 512           
SHEET    7 AC6 8 THR C 589  SER C 594  1  O  LEU C 590   N  ALA C 533           
SHEET    8 AC6 8 VAL C 619  PHE C 624  1  O  ARG C 620   N  ILE C 591           
SHEET    1 AC7 4 PHE D  19  VAL D  25  0                                        
SHEET    2 AC7 4 VAL D  32  GLN D  38 -1  O  ALA D  33   N  GLN D  24           
SHEET    3 AC7 4 ARG D  57  SER D  63 -1  O  TRP D  61   N  PHE D  34           
SHEET    4 AC7 4 ARG D  69  PRO D  70 -1  O  ARG D  69   N  LEU D  62           
SHEET    1 AC8 4 GLY D  79  TRP D  85  0                                        
SHEET    2 AC8 4 ASN D  91  SER D  97 -1  O  VAL D  95   N  SER D  81           
SHEET    3 AC8 4 ALA D 104  PRO D 109 -1  O  MET D 106   N  PHE D  94           
SHEET    4 AC8 4 ARG D 116  ARG D 117 -1  O  ARG D 116   N  LEU D 107           
SHEET    1 AC9 4 SER D 126  TRP D 130  0                                        
SHEET    2 AC9 4 PHE D 136  THR D 140 -1  O  ALA D 138   N  GLN D 129           
SHEET    3 AC9 4 LEU D 178  ASP D 182 -1  O  TRP D 179   N  PHE D 139           
SHEET    4 AC9 4 LYS D 187  TYR D 192 -1  O  TYR D 192   N  LEU D 178           
SHEET    1 AD1 4 LEU D 201  TRP D 203  0                                        
SHEET    2 AD1 4 GLY D 209  GLN D 214 -1  O  LEU D 211   N  SER D 202           
SHEET    3 AD1 4 GLN D 226  PRO D 232 -1  O  TYR D 229   N  ILE D 212           
SHEET    4 AD1 4 GLN D 243  SER D 250 -1  O  LEU D 245   N  VAL D 228           
SHEET    1 AD2 4 ALA D 252  PRO D 257  0                                        
SHEET    2 AD2 4 PHE D 264  GLY D 268 -1  O  ILE D 267   N  HIS D 253           
SHEET    3 AD2 4 HIS D 280  GLU D 285 -1  O  ILE D 284   N  PHE D 264           
SHEET    4 AD2 4 GLN D 288  ARG D 291 -1  O  ARG D 290   N  LEU D 283           
SHEET    1 AD3 4 ARG D 318  TRP D 319  0                                        
SHEET    2 AD3 4 THR D 324  VAL D 331 -1  O  LEU D 326   N  ARG D 318           
SHEET    3 AD3 4 SER D 334  HIS D 341 -1  O  PHE D 338   N  PHE D 327           
SHEET    4 AD3 4 GLY D 344  ASP D 350 -1  O  ASP D 350   N  LEU D 337           
SHEET    1 AD4 4 GLY D 355  ALA D 362  0                                        
SHEET    2 AD4 4 VAL D 367  SER D 373 -1  O  GLU D 372   N  VAL D 356           
SHEET    3 AD4 4 ARG D 376  LEU D 382 -1  O  GLU D 381   N  LEU D 369           
SHEET    4 AD4 4 GLN D 385  ARG D 386 -1  O  GLN D 385   N  LEU D 382           
SHEET    1 AD5 8 GLN D 402  THR D 408  0                                        
SHEET    2 AD5 8 GLY D 411  LEU D 418 -1  O  GLY D 413   N  PHE D 406           
SHEET    3 AD5 8 GLY D 457  SER D 461 -1  O  VAL D 458   N  LEU D 418           
SHEET    4 AD5 8 VAL D 426  ILE D 432  1  N  LEU D 429   O  GLY D 457           
SHEET    5 AD5 8 LEU D 503  GLY D 513  1  O  ALA D 509   N  LEU D 430           
SHEET    6 AD5 8 ALA D 532  ASP D 536  1  O  ASP D 536   N  GLY D 512           
SHEET    7 AD5 8 THR D 589  SER D 594  1  O  LEU D 590   N  ALA D 533           
SHEET    8 AD5 8 VAL D 619  PHE D 624  1  O  ARG D 620   N  ILE D 591           
CISPEP   1 GLY A  435    PRO A  436          0         4.09                     
CISPEP   2 GLY B  435    PRO B  436          0         3.45                     
CISPEP   3 GLY C  435    PRO C  436          0         3.87                     
CISPEP   4 GLY D  435    PRO D  436          0         3.42                     
SITE     1 AC1  6 GLY A 434  GLY A 435  SER A 514  TYR A 515                    
SITE     2 AC1  6 PHE A 555  ARG A 599                                          
SITE     1 AC2  5 GLY B 434  GLY B 435  SER B 514  TYR B 515                    
SITE     2 AC2  5 ARG B 599                                                     
SITE     1 AC3  5 GLY C 434  GLY C 435  SER C 514  TYR C 515                    
SITE     2 AC3  5 ARG C 599                                                     
SITE     1 AC4  5 GLY D 434  GLY D 435  SER D 514  TYR D 515                    
SITE     2 AC4  5 ARG D 599                                                     
CRYST1   73.702  195.092  107.715  90.00  99.97  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013568  0.000000  0.002385        0.00000                         
SCALE2      0.000000  0.005126  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009426        0.00000                         
TER    4634      LEU A 655                                                      
TER    9262      LEU B 655                                                      
TER   13823      LEU C 655                                                      
TER   18370      LEU D 655                                                      
MASTER      641    0    4   56  144    0    8    619423    4   16  204          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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